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Entry version 139 (08 May 2019)
Sequence version 2 (07 Jul 2009)
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Protein

HTH-type transcriptional regulator MntR

Gene

mntR

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Central regulator of manganese homeostasis that regulates the expression of both manganese uptake and efflux systems (PubMed:27748968, PubMed:10760146, PubMed:12950915). In the presence of high levels of manganese, it mediates repression of the manganese uptake systems MntH and MntABCD and activation of the efflux systems MneP and MneS. Binds with high affinity to the regulatory regions of its target genes (PubMed:27748968, PubMed:12950915). The manganese concentration required for activation of efflux is higher than that for repression of uptake (PubMed:27748968).3 Publications

Caution

Was originally thought to act as an activator for the mntABCD operon.2 Publications

<p>This subsection of the ‘Function’ section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

DNA binding is strongly activated by Mn2+ and Cd2+, but it is poorly activated by non-cognate metal cations, including Co2+, Fe2+, Ni2+, Ca2+ and Zn2+. In the strict absence of divalent transition metal ions, MntR has a low affinity for DNA.3 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi8Manganese or cadmium 13 Publications1
Metal bindingi11Manganese or cadmium 23 Publications1
Metal bindingi77Manganese or cadmium 2; via pros nitrogen3 Publications1
Metal bindingi99Manganese or cadmium 12 Publications1
Metal bindingi99Manganese or cadmium 23 Publications1
Metal bindingi102Manganese or cadmium 13 Publications1
Metal bindingi102Manganese or cadmium 23 Publications1
Metal bindingi103Manganese or cadmium 1; via tele nitrogen3 Publications1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionActivator, DNA-binding, Repressor
Biological processTranscription, Transcription regulation
LigandCadmium, Manganese, Metal-binding

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
BSUB:BSU24520-MONOMER

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
HTH-type transcriptional regulator MntRUniRule annotationCurated
Alternative name(s):
Manganese transport regulator1 PublicationUniRule annotation
Manganese(II) metalloregulatory protein MntR1 Publication
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:mntR1 PublicationUniRule annotation
Synonyms:yqhN
Ordered Locus Names:BSU24520
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiBacillus subtilis (strain 168)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri224308 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000001570 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

GO - Cellular componenti

Keywords - Cellular componenti

Cytoplasm

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the ‘Pathology and Biotech’ section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

Null mutant is very sensitive to manganese (PubMed:27748968, PubMed:10760146). Mutant also displays increased sensitivity to cadmium (PubMed:10760146).2 Publications

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi8D → M: Binds only one manganese ion, in a pseudo-hexacoordinate geometry. 1 Publication1
Mutagenesisi11E → K: Retains selectivity for activation by Mn(2+) and Cd(2+) over Co(2+) and Fe(2+). Can bind Mn(2+) in the C site, despite alteration to the A site, and adopt active DNA-binding conformations. Non-cognate ions fail to generate fully active complexes. 1 Publication1
Mutagenesisi77H → A: Retains selectivity for activation by Mn(2+) and Cd(2+) over Co(2+) and Fe(2+). Can bind Mn(2+) in the C site, despite alteration to the A site, and adopt active DNA-binding conformations. Non-cognate ions fail to generate fully active complexes. 1 Publication1

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00002011181 – 142HTH-type transcriptional regulator MntRAdd BLAST142

Proteomic databases

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
P54512

PRoteomics IDEntifications database

More...
PRIDEi
P54512

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homodimer.UniRule annotation5 Publications

GO - Molecular functioni

Protein-protein interaction databases

STRING: functional protein association networks

More...
STRINGi
224308.BSU24520

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1142
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1ON1X-ray1.75A/B1-142[»]
1ON2X-ray1.61A/B1-142[»]
2EV0X-ray1.65A/B1-142[»]
2EV5X-ray2.00A/B1-142[»]
2EV6X-ray1.70A/B1-142[»]
2F5CX-ray2.40A1-142[»]
2F5DX-ray1.90A/B1-142[»]
2F5EX-ray2.20A/B1-142[»]
2F5FX-ray2.40A/B1-142[»]
2HYFX-ray2.80A/B/C/D1-142[»]
2HYGX-ray2.80D1-142[»]
3R60X-ray1.80A/B2-142[»]
3R61X-ray1.90A/B2-142[»]
4HV5X-ray1.90A/B2-142[»]
4HV6X-ray2.30A/B2-142[»]
4HX4X-ray1.65A/B2-142[»]
4HX7X-ray1.90A/B2-142[»]
4HX8X-ray2.00A/B2-142[»]

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
P54512

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P54512

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini1 – 63HTH dtxR-typeUniRule annotationAdd BLAST63

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

Contains an N-terminal DNA-binding domain and a C-terminal dimerization domain (PubMed:12847518, PubMed:16533030, PubMed:23298157). Contains two metal binding sites per subunit, site A (corresponding to metal ion 2) and site C (corresponding to metal ion 1), which both contribute to the metal selectivity of MntR. A large metal cation is needed at the A site to correctly orient and position the C site ligands. Smaller, non-cognate metal cations bind at the A site, but disrupt the C site, blocking the full activation of MntR. Binding at the C site also favors Mn(2+) and Cd(2+) over other metals (PubMed:16533030, PubMed:23298157).3 Publications

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the DtxR/MntR family.UniRule annotationCurated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG4105KST Bacteria
COG1321 LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000040349

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P54512

Identification of Orthologs from Complete Genome Data

More...
OMAi
CIIERFL

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P54512

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
1.10.10.10, 1 hit
1.10.60.10, 1 hit

HAMAP database of protein families

More...
HAMAPi
MF_00732 HTH_MntR, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR001367 Fe_dep_repressor
IPR036421 Fe_dep_repressor_sf
IPR022687 HTH_DTXR
IPR022897 HTH_tscrpt_reg_MntR
IPR022689 Iron_dep_repressor
IPR036388 WH-like_DNA-bd_sf
IPR036390 WH_DNA-bd_sf

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF02742 Fe_dep_repr_C, 1 hit
PF01325 Fe_dep_repress, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00529 HTH_DTXR, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF46785 SSF46785, 1 hit
SSF47979 SSF47979, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS50944 HTH_DTXR, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

P54512-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MTTPSMEDYI EQIYMLIEEK GYARVSDIAE ALAVHPSSVT KMVQKLDKDE
60 70 80 90 100
YLIYEKYRGL VLTSKGKKIG KRLVYRHELL EQFLRIIGVD EEKIYNDVEG
110 120 130 140
IEHHLSWNSI DRIGDLVQYF EEDDARKKDL KSIQKKTEHH NQ
Length:142
Mass (Da):16,759
Last modified:July 7, 2009 - v2
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i653BD8E0F4AB9F2C
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti81E → D in BAA12551 (PubMed:8969508).Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
D84432 Genomic DNA Translation: BAA12551.1
AL009126 Genomic DNA Translation: CAB14383.2

Protein sequence database of the Protein Information Resource

More...
PIRi
E69959

NCBI Reference Sequences

More...
RefSeqi
NP_390332.2, NC_000964.3
WP_003236923.1, NZ_JNCM01000036.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
CAB14383; CAB14383; BSU24520

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
938554

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
bsu:BSU24520

Pathosystems Resource Integration Center (PATRIC)

More...
PATRICi
fig|224308.179.peg.2670

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D84432 Genomic DNA Translation: BAA12551.1
AL009126 Genomic DNA Translation: CAB14383.2
PIRiE69959
RefSeqiNP_390332.2, NC_000964.3
WP_003236923.1, NZ_JNCM01000036.1

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1ON1X-ray1.75A/B1-142[»]
1ON2X-ray1.61A/B1-142[»]
2EV0X-ray1.65A/B1-142[»]
2EV5X-ray2.00A/B1-142[»]
2EV6X-ray1.70A/B1-142[»]
2F5CX-ray2.40A1-142[»]
2F5DX-ray1.90A/B1-142[»]
2F5EX-ray2.20A/B1-142[»]
2F5FX-ray2.40A/B1-142[»]
2HYFX-ray2.80A/B/C/D1-142[»]
2HYGX-ray2.80D1-142[»]
3R60X-ray1.80A/B2-142[»]
3R61X-ray1.90A/B2-142[»]
4HV5X-ray1.90A/B2-142[»]
4HV6X-ray2.30A/B2-142[»]
4HX4X-ray1.65A/B2-142[»]
4HX7X-ray1.90A/B2-142[»]
4HX8X-ray2.00A/B2-142[»]
SMRiP54512
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi224308.BSU24520

Proteomic databases

PaxDbiP54512
PRIDEiP54512

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB14383; CAB14383; BSU24520
GeneIDi938554
KEGGibsu:BSU24520
PATRICifig|224308.179.peg.2670

Phylogenomic databases

eggNOGiENOG4105KST Bacteria
COG1321 LUCA
HOGENOMiHOG000040349
InParanoidiP54512
OMAiCIIERFL
PhylomeDBiP54512

Enzyme and pathway databases

BioCyciBSUB:BSU24520-MONOMER

Miscellaneous databases

EvolutionaryTraceiP54512

Family and domain databases

Gene3Di1.10.10.10, 1 hit
1.10.60.10, 1 hit
HAMAPiMF_00732 HTH_MntR, 1 hit
InterProiView protein in InterPro
IPR001367 Fe_dep_repressor
IPR036421 Fe_dep_repressor_sf
IPR022687 HTH_DTXR
IPR022897 HTH_tscrpt_reg_MntR
IPR022689 Iron_dep_repressor
IPR036388 WH-like_DNA-bd_sf
IPR036390 WH_DNA-bd_sf
PfamiView protein in Pfam
PF02742 Fe_dep_repr_C, 1 hit
PF01325 Fe_dep_repress, 1 hit
SMARTiView protein in SMART
SM00529 HTH_DTXR, 1 hit
SUPFAMiSSF46785 SSF46785, 1 hit
SSF47979 SSF47979, 1 hit
PROSITEiView protein in PROSITE
PS50944 HTH_DTXR, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiMNTR_BACSU
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P54512
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: July 7, 2009
Last modified: May 8, 2019
This is version 139 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
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